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Q9P996

- PSB_ARCFU

UniProt

Q9P996 - PSB_ARCFU

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Protein

Proteasome subunit beta

Gene
psmB, AF_0481
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation By similarity.UniRule annotation

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.UniRule annotation

Enzyme regulationi

The formation of the proteasomal ATPase PAN-20S proteasome complex, via the docking of the C-termini of PAN into the intersubunit pockets in the alpha-rings, triggers opening of the gate for substrate entry. Interconversion between the open-gate and close-gate conformations leads to a dynamic regulation of the 20S proteasome proteolysis activity By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121Nucleophile By similarity

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. proteasomal protein catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciAFUL224325:GJBC-494-MONOMER.

Protein family/group databases

MEROPSiT01.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta (EC:3.4.25.1)
Alternative name(s):
20S proteasome beta subunit
Proteasome core protein PsmB
Gene namesi
Name:psmB
Ordered Locus Names:AF_0481
OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifieri224325 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
ProteomesiUP000002199: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. proteasome core complex, beta-subunit complex Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1111Removed in mature form; by autocatalysis By similarityPRO_0000026659Add
BLAST
Chaini12 – 213202Proteasome subunit betaUniRule annotationPRO_0000026660Add
BLAST

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

The 20S proteasome core is composed of 14 alpha and 14 beta subunits that assemble into four stacked heptameric rings, resulting in a barrel-shaped structure. The two inner rings, each composed of seven catalytic beta subunits, are sandwiched by two outer rings, each composed of seven alpha subunits. The catalytic chamber with the active sites is on the inside of the barrel. Has probably a gated structure, the ends of the cylinder being occluded by the N-termini of the alpha-subunits. Is likely capped at one or both ends by the proteasome regulatory ATPase, PAN.1 Publication

Protein-protein interaction databases

IntActiQ9P996. 1 interaction.
STRINGi224325.AF0481.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196
Beta strandi22 – 287
Beta strandi31 – 333
Beta strandi36 – 416
Beta strandi45 – 495
Beta strandi52 – 587
Helixi60 – 8122
Helixi87 – 10014
Turni101 – 1033
Beta strandi108 – 1169
Beta strandi119 – 1257
Beta strandi131 – 14111
Helixi144 – 15411
Helixi161 – 17616
Beta strandi186 – 1916
Beta strandi196 – 1983
Helixi200 – 2078
Helixi208 – 2103

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2QX-ray2.83H/I/J/K/L/M/N12-213[»]
ProteinModelPortaliQ9P996.
SMRiQ9P996. Positions 12-213.

Miscellaneous databases

EvolutionaryTraceiQ9P996.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
KOiK03433.
OMAiMVDWLGT.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
HAMAPiMF_02113_A. Proteasome_B_A.
InterProiIPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR03634. arc_protsome_B. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9P996-1 [UniParc]FASTAAdd to Basket

« Hide

MSMIEEKIYK GTTTVGLVCK DGVVMATEKR ATMGNFIASK AAKKIYQIAD    50
RMAMTTAGSV GDAQFLARII KIEANLYEIR RERKPTVRAI ATLTSNLLNS 100
YRYFPYLVQL LIGGIDSEGK SIYSIDPIGG AIEEKDIVAT GSGSLTAYGV 150
LEDRFTPEIG VDEAVELAVR AIYSAMKRDS ASGDGIDVVK ITEDEFYQYS 200
PEEVEQILAK FRK 213
Length:213
Mass (Da):23,418
Last modified:October 1, 2000 - v1
Checksum:iDA03E480A88F8227
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB90757.1.
PIRiA69310.
RefSeqiNP_069317.1. NC_000917.1.

Genome annotation databases

EnsemblBacteriaiAAB90757; AAB90757; AF_0481.
GeneIDi1483698.
KEGGiafu:AF0481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000782 Genomic DNA. Translation: AAB90757.1 .
PIRi A69310.
RefSeqi NP_069317.1. NC_000917.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J2Q X-ray 2.83 H/I/J/K/L/M/N 12-213 [» ]
ProteinModelPortali Q9P996.
SMRi Q9P996. Positions 12-213.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9P996. 1 interaction.
STRINGi 224325.AF0481.

Protein family/group databases

MEROPSi T01.002.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB90757 ; AAB90757 ; AF_0481 .
GeneIDi 1483698.
KEGGi afu:AF0481.

Phylogenomic databases

eggNOGi COG0638.
KOi K03433.
OMAi MVDWLGT.

Enzyme and pathway databases

BioCyci AFUL224325:GJBC-494-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9P996.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
HAMAPi MF_02113_A. Proteasome_B_A.
InterProi IPR029055. Ntn_hydrolases_N.
IPR019983. Pept_T1A_Psome_bsu_arc.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR03634. arc_protsome_B. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
    Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
    , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
    Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
  2. "Investigations on the maturation and regulation of archaebacterial proteasomes."
    Groll M., Brandstetter H., Bartunik H., Bourenkow G., Huber R.
    J. Mol. Biol. 327:75-83(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 12-213 IN COMPLEX WITH ALPHA SUBUNIT AND CALPAIN-INHIBITOR I, SUBUNIT.

Entry informationi

Entry nameiPSB_ARCFU
AccessioniPrimary (citable) accession number: Q9P996
Secondary accession number(s): O29769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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